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| | <StructureSection load='5k9t' size='340' side='right'caption='[[5k9t]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5k9t' size='340' side='right'caption='[[5k9t]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k9t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K9T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5K9T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k9t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_55989 Escherichia coli 55989]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K9T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5k9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9t OCA], [http://pdbe.org/5k9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k9t RCSB], [http://www.ebi.ac.uk/pdbsum/5k9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9t ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5k9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9t OCA], [https://pdbe.org/5k9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k9t RCSB], [https://www.ebi.ac.uk/pdbsum/5k9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SECA_ECO55 SECA_ECO55]] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | + | [https://www.uniprot.org/uniprot/SECA_ECOLI SECA_ECOLI] Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.<ref>PMID:15140892</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia coli 55989]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Shilton, B H]] | + | [[Category: Shilton BH]] |
| - | [[Category: Vezina, G C]] | + | [[Category: Vezina GC]] |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: C-terminal truncation]]
| + | |
| - | [[Category: N-terminus]]
| + | |
| - | [[Category: Peptide binding]]
| + | |
| - | [[Category: Preprotein translocase]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Seca-n68]]
| + | |
| Structural highlights
Function
SECA_ECOLI Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.[1]
Publication Abstract from PubMed
SecA is the ATPase of preprotein translocase. SecA is a dimer in solution and changes in its oligomeric state may function in preprotein translocation. The SecA-N68 construct, in which the C-terminal helical domains of SecA are deleted, was used to investigate the mechanism of SecA oligomerization. SecA-N68 is in equilibrium between monomers, dimers, and tetramers. Subunit interactions in the SecA-N68 tetramer are mediated entirely by unstructured regions at its N- and C-termini: when the termini are deleted to yield SecA-N68NC, the construct is completely monomeric. This monomeric construct yielded crystals diffracting to 2.6 A that were used to solve the structure of SecA-N68, including the "preprotein crosslinking domain" (PPXD) that was missing from previous E. coli SecA structures. The SecA-N68 structure was combined with small angle X-ray scattering (SAXS) data to construct a model of the SecA-N68 tetramer that is consistent with the essential roles of the extreme N- and C-termini in oligomerization. This mode of oligomerization, which depends on binding of the extreme N-terminus to the DEAD motor domains, NBD1 and NBD2, was used to model a novel parallel and flexible SecA solution dimer that agrees well with SAXS data.
An alternate mode of oligomerization for E. coli SecA.,Yazdi AK, Vezina GC, Shilton BH Sci Rep. 2017 Sep 18;7(1):11747. doi: 10.1038/s41598-017-11648-5. PMID:28924213[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Froderberg L, Houben EN, Baars L, Luirink J, de Gier JW. Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. J Biol Chem. 2004 Jul 23;279(30):31026-32. Epub 2004 May 12. PMID:15140892 doi:10.1074/jbc.M403229200
- ↑ Yazdi AK, Vezina GC, Shilton BH. An alternate mode of oligomerization for E. coli SecA. Sci Rep. 2017 Sep 18;7(1):11747. doi: 10.1038/s41598-017-11648-5. PMID:28924213 doi:http://dx.doi.org/10.1038/s41598-017-11648-5
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